MolNFT v1 · #176371 · protein
Silk worm fkbp, isoform-1
7DKI · Peptidylprolyl isomerase: “Silk worm fkbp, isoform-1”. X-ray diffraction, 2 pockets (best druggability 0.39). MolNFT v1 #176371 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7DKI
- Type
- protein
- Length
- 214 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidylprolyl isomerase
- EC
- 5.2.1.8
- UniProt
- Q1HQ55
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peptidylprolyl isomerase (EC 5.2.1.8) | protein | 107 | 13% helix, 40% strand | Q1HQ55 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.39 | 0.74 | 26 | empty |
| 2 | 59 | 0.29 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 289 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7DKI · Silk worm FKBP, isoform-1 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q1HQ55
- Elsewhere: RCSB PDB 7DKI · PDBe 7DKI · UniProt Q1HQ55
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